Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data.
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Phosphorylation of Single Stranded RNA Virus Proteins and Potential for Novel Therapeutic StrategiesEvolution and functional cross-talk of protein post-translational modificationsPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Reproducible Analysis of Post-Translational Modifications in Proteomes--Application to Human MutationsGlobal identification and characterization of both O-GlcNAcylation and phosphorylation at the murine synapseTurnover of protein phosphorylation evolving under stabilizing selectionAn allosteric conduit facilitates dynamic multisite substrate recognition by the SCF(Cdc4) ubiquitin ligaseSpatial proximity statistics suggest a regulatory role of protein phosphorylation on compound binding.Towards understanding the crosstalk between protein post-translational modifications: Homo- and heterotypic PTM pair distances on protein surfaces are not random.Phosphorylation variation during the cell cycle scales with structural propensities of proteins.Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes.Phosphopeptide enrichment by covalent chromatography after derivatization of protein digests immobilized on reversed-phase supportsCo-occurring protein phosphorylation are functionally associated.Functional analysis of phosphorylation on Saccharomyces cerevisiae syntaxin 1 homologues Sso1p and Sso2p.Physicochemical mechanisms of protein regulation by phosphorylation.Phosphorylation in protein-protein binding: effect on stability and function.A Proteome-wide Domain-centric Perspective on Protein Phosphorylation.Evolutionary patterns of phosphorylated serinesDual coordination of post translational modifications in human protein networks.Crosstalk between signaling pathways provided by single and multiple protein phosphorylation sitesCyclic GMP kinase II (cGKII) inhibits NHE3 by altering its trafficking and phosphorylating NHE3 at three required sites: identification of a multifunctional phosphorylation siteSingle-step inline hydroxyapatite enrichment facilitates identification and quantitation of phosphopeptides from mass-limited proteomes with MudPITCharacterization and Prediction of Protein Phosphorylation Hotspots in Arabidopsis thalianaSystematic Analysis and Prediction of In Situ Cross Talk of O-GlcNAcylation and Phosphorylation.Minimal models for cell-cycle control based on competitive inhibition and multisite phosphorylations of Cdk substrates.EGF-receptor specificity for phosphotyrosine-primed substrates provides signal integration with SrcSysPTM 2.0: an updated systematic resource for post-translational modification.The role of structural disorder in cell cycle regulation, related clinical proteomics, disease development and drug targeting.Cell cycle phosphorylation of mitotic exit network (MEN) proteins.Hydrogen bond based smart polymer for highly selective and tunable capture of multiply phosphorylated peptides.Evaluation and properties of the budding yeast phosphoproteome.Evolution of signal multiplexing by 14-3-3-binding 2R-ohnologue protein families in the vertebrates.A cell cycle phosphoproteome of the yeast centrosome.Site-specific NMR mapping and time-resolved monitoring of serine and threonine phosphorylation in reconstituted kinase reactions and mammalian cell extracts.Recent advances in phosphoproteomics and application to neurological diseases.A tri-serine cluster within the topoisomerase IIα-interaction domain of the BLM helicase is required for regulating chromosome breakage in human cells.Defeating major contaminants in Fe3+-IMAC phosphopeptide enrichment.Characterization and application studies of ProxyPhos, a chemosensor for the detection of proximally phosphorylated peptides and proteins in aqueous solutions.PTM-ssMP: A Web Server for Predicting Different Types of Post-translational Modification Sites Using Novel Site-specific Modification Profile.The Challenges of Interpreting Phosphoproteomics Data: A Critical View Through the Bioinformatics Lens
P2860
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P2860
Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Cooperativity within proximal ...... m large-scale proteomics data.
@ast
Cooperativity within proximal ...... m large-scale proteomics data.
@en
Cooperativity within proximal ...... m large-scale proteomics data.
@nl
type
label
Cooperativity within proximal ...... m large-scale proteomics data.
@ast
Cooperativity within proximal ...... m large-scale proteomics data.
@en
Cooperativity within proximal ...... m large-scale proteomics data.
@nl
prefLabel
Cooperativity within proximal ...... m large-scale proteomics data.
@ast
Cooperativity within proximal ...... m large-scale proteomics data.
@en
Cooperativity within proximal ...... m large-scale proteomics data.
@nl
P2860
P356
P1433
P1476
Cooperativity within proximal ...... m large-scale proteomics data.
@en
P2093
Regev Schweiger
P2860
P2888
P356
10.1186/1745-6150-5-6
P577
2010-01-26T00:00:00Z
P5875
P6179
1001099836